PPT1_RAT
ID PPT1_RAT Reviewed; 306 AA.
AC P45479; A0JN20;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Palmitoyl-protein thioesterase 1;
DE Short=PPT-1;
DE EC=3.1.2.22;
DE AltName: Full=Palmitoyl-protein hydrolase 1;
DE Flags: Precursor;
GN Name=Ppt1; Synonyms=Cln1, Ppt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7916016; DOI=10.1016/s0021-9258(17)31641-1;
RA Camp L.A., Verkruyse L.A., Afendis S.J., Slaughter C.A., Hofmann S.L.;
RT "Molecular cloning and expression of palmitoyl-protein thioesterase.";
RL J. Biol. Chem. 269:23212-23219(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 61-74; 105-122; 128-174; 180-196; 217-224; 254-268 AND
RP 286-294, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate
CC from modified cysteine residues in proteins or peptides during
CC lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
CC {ECO:0000250|UniProtKB:P45478}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:P45478};
CC -!- SUBUNIT: Interacts with CLN5, ATP5F1A and ATP5F1B.
CC {ECO:0000250|UniProtKB:O88531}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P45478}. Secreted
CC {ECO:0000269|PubMed:7916016}.
CC -!- TISSUE SPECIFICITY: Highest amounts in brain, testis, lung, and spleen.
CC Lowest amounts in liver and skeletal muscle.
CC {ECO:0000269|PubMed:7916016}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P45478}.
CC -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC {ECO:0000305}.
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DR EMBL; L34262; AAA59358.1; -; mRNA.
DR EMBL; BC126089; AAI26090.1; -; mRNA.
DR PIR; A54717; A54717.
DR RefSeq; NP_071947.1; NM_022502.2.
DR AlphaFoldDB; P45479; -.
DR SMR; P45479; -.
DR IntAct; P45479; 1.
DR STRING; 10116.ENSRNOP00000017998; -.
DR ESTHER; ratno-ppt; Palmitoyl-protein_thioesterase.
DR GlyGen; P45479; 3 sites.
DR jPOST; P45479; -.
DR PaxDb; P45479; -.
DR PRIDE; P45479; -.
DR Ensembl; ENSRNOT00000112154; ENSRNOP00000091845; ENSRNOG00000012616.
DR GeneID; 29411; -.
DR KEGG; rno:29411; -.
DR UCSC; RGD:61994; rat.
DR CTD; 5538; -.
DR RGD; 61994; Ppt1.
DR eggNOG; KOG2541; Eukaryota.
DR GeneTree; ENSGT00940000156790; -.
DR HOGENOM; CLU_050129_0_0_1; -.
DR InParanoid; P45479; -.
DR OMA; FFIHPNE; -.
DR OrthoDB; 904122at2759; -.
DR PhylomeDB; P45479; -.
DR TreeFam; TF323926; -.
DR BRENDA; 3.1.2.22; 5301.
DR Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:P45479; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012616; Expressed in spleen and 18 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISO:RGD.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0044265; P:cellular macromolecule catabolic process; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0031579; P:membrane raft organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0006907; P:pinocytosis; ISO:RGD.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0032429; P:regulation of phospholipase A2 activity; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:RGD.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002472; Palm_thioest.
DR InterPro; IPR030294; PPT1.
DR PANTHER; PTHR11247:SF8; PTHR11247:SF8; 1.
DR PRINTS; PR00414; PPTHIESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CHAIN 28..306
FT /note="Palmitoyl-protein thioesterase 1"
FT /id="PRO_0000025553"
FT ACT_SITE 115
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 233
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT ACT_SITE 289
FT /evidence="ECO:0000250|UniProtKB:P45478"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..46
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 96..128
FT /evidence="ECO:0000250|UniProtKB:P50897"
FT DISULFID 152..160
FT /evidence="ECO:0000250|UniProtKB:P50897"
SQ SEQUENCE 306 AA; 34455 MW; 232F917A21738F2E CRC64;
MASPGYRRLL AAALLPWCCA AWALGHLDPP SPPPLVIWHG MGDSCCNPMS MGSIKKMVEK
EIPGIYVLSL EIGKNMVEDV ENSFFLNVNL QVGMACQILE KDPKLQHGYN AIGFSQGGQF
LRAVAQRCPT PPMMTLISVG GQHQGVFGLP RCPGESSHIC DFIRKSLNAG AYSKVVQERL
VQAQYWHDPI KEEVYRNCSI FLADINQERH INESYKENLM ALKKFVMVKF FNDSIVDPVD
SEWFGFYRSG QAKETIPLQE TTLYTEDRLG LKKMDKAGKL VFLAKEGDHL QISKEWFTAH
IIPFLK
